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Bacteriocin ASM1 is an O / S ‐diglycosylated, plasmid‐encoded homologue of glycocin F

Authors :
Trevor S. Loo
Gillian E. Norris
Vladimír Havlíček
Patrick Main
Tomomi Hata
Petr Man
Mark L. Patchett
Petr Novák
Source :
FEBS Letters. 594:1196-1206
Publication Year :
2020
Publisher :
Wiley, 2020.

Abstract

Here, we report on the biochemical characterization of a new glycosylated bacteriocin (glycocin), ASM1, produced by Lactobacillus plantarum A-1 and analysis of the A-1 bacteriocinogenic genes. ASM1 is 43 amino acids in length with Ser18-O- and Cys43-S-linked N-acetylglucosamine moieties that are essential for its inhibitory activity. Its only close homologue, glycocin F (GccF), has five amino acid substitutions all residing in the flexible C-terminal 'tail' and a lower IC50 (0.9 nm) compared to that of ASM1 (1.5 nm). Asm/gcc genes share the same organization (asmH← →asmABCDE→F), and the asm genes reside on an 11 905-bp plasmid dedicated to ASM1 production. The A-1 genome also harbors a gene encoding a 'rare' bactofencin-type bacteriocin. As more examples of prokaryote S-GlcNAcylation are discovered, the functions of this modification may be understood.

Details

ISSN :
18733468 and 00145793
Volume :
594
Database :
OpenAIRE
Journal :
FEBS Letters
Accession number :
edsair.doi.dedup.....9fa05e3e1d54c4f9ce05f9d4d90d3163
Full Text :
https://doi.org/10.1002/1873-3468.13708